Abstract
Guinea pig and human macrophage migration inhibitory factors (MIF) were modified by reduction and alkylation. Guinea pig MIF lost activity when reduced and alkylated in the presence of urea or guanidine. Irreversible sulfhydryl modification was dependent upon the denaturation of the MIF molecule, suggesting that sulfhydryl bonds within the native molecule may contribute to biologic activity. Alkylation alone in guanidine had no effect on biologic activity, suggesting that free sulfhydryl groups are not essential for migration inhibitory activity. In contrast, human MIF was unaffected by any of the procedures used. Since previous studies have shown that human MIF can dissociate during extensive dialysis, these observations suggest that sulfyhydryl bonds are not important in the expression of human migration inhibitory activity. We have also shown that skin reactive factor (SRF), another lymphokine activity present in the activated lymphocyte culture supernates studied, has a pattern of susceptibility to reduction-alkylation procedures which is similar to that of MIF.
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